The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER.
The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER.
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DOI：
10.1016/j.molcel.2009.09.016
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发表时间：
2009-10-09
期刊：
影响因子：
16
通讯作者：
Schlieker, Christian
中科院分区：
文献类型：
--
作者：
Ernst, Robert;Mueller, Britta;Ploegh, Hidde L.;Schlieker, Christian
YOD 1是卵巢肿瘤（otubain）家族中高度保守的去泛素化酶，其功能尚未在哺乳动物细胞中分配。YOD 1是以p97为核的多蛋白复合物的组成部分，表明与负责错误折叠蛋白质从内质网移位的途径有功能联系。YOD 1变体的表达剥夺了其去泛素化活性，从而使位错反应停止，这是通过各种位错底物的稳定性来判断的。因此，我们观察到与p97在胞质溶胶中的多聚泛素化的位错中间体的增加。这种显性负效应依赖于分别附加到催化otubain核心结构域的N-和C-末端的UBX和锌指结构域。将p97相关的泛素加工功能分配给YOD 1增加了我们对p97在位错过程中的作用的理解。
YOD1 is a highly conserved deubiquitinating enzyme of the ovarian tumor (otubain) family, whose function has yet to be assigned in mammalian cells. YOD1 is a constituent of a multiprotein complex with p97 as its nucleus, suggesting a functional link to a pathway responsible for the dislocation of misfolded proteins from the endoplasmic reticulum. Expression of a YOD1 variant deprived of its deubiquitinating activity imposes a halt on the dislocation reaction, as judged by the stabilization of various dislocation substrates. Accordingly, we observe an increase in polyubiquitinated dislocation intermediates in association with p97 in the cytosol. This dominant negative effect is dependent on the UBX and Zinc finger domains, appended to the N- and C-terminus of the catalytic otubain core domain, respectively. The assignment of a p97-associated ubiquitin processing function to YOD1 adds to our understanding of p97’s role in the dislocation process.
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影响因子：
16.8
作者：
Martin, Andreas;Baker, Tania A.;Sauer, Robert T.
通讯作者：
Sauer, Robert T.
DOI：
10.1038/nsb972
发表时间：
2003-10-01
期刊：
NATURE STRUCTURAL BIOLOGY
影响因子：
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